The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety.

摘要: The lecticans are a family of chondroitin sulfate proteoglycans including aggrecan, versican, neurocan, and brevican. C-terminal globular domains structurally related to selectins, consisting C-type lectin domain flanked by epidermal growth factor complement regulatory protein domains. versican has been shown bind tenascin-R, an extracellular matrix specifically expressed in the nervous system, interaction was presumed be mediated carbohydrate-protein interaction. In this paper, we show that brevican, another lectican is also binds tenascin-R. Surprisingly, protein-protein through fibronectin type III 3-5 independent any carbohydrates or sulfated amino acids. other same tenascin-R interactions. Surface plasmon resonance analysis revealed brevican at least 10-fold higher affinity than lectins. Tenascin-R coprecipitated with from adult rat brain extracts, suggesting form complexes vivo. These results demonstrate can interact interactions, suggest physiological ligand brain.